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J. Biol. Chem., Vol. 265, Issue 7, 3815-3822, Mar, 1990
LK Jennings, CF Fox, WC Kouns, CP McKay, LR Ballou and HE Schultz
Anti-human platelet p24/CD9 (p24/monoclonal antibody 7) causes the
activation of platelets and in the presence of calcium induces platelet
aggregation. Our studies suggest that platelet response to this antibody is
mediated at least in part by the pertussis toxin-sensitive guanine
nucleotide-binding proteins (G proteins) that stimulate phosphoinositide
hydrolysis and inhibit adenylate cyclase. Prior exposure of saponin-treated
platelets to anti-p24/CD9 inhibited the [32P] ADP-ribosylation of the alpha
41 protein by pertussis toxin. Platelet aggregation induced by this
antibody is preceded by and/or accompanied by accelerated
phosphatidylinositol turnover, the generation of inositol phosphates and
diacylglycerol (DAG), calcium mobilization, and protein phosphorylation.
The production of inositol phosphate(s) was measurable within 15 s of
either anti-p24/CD9 or thrombin addition. Within 10 s of antibody addition
(10 micrograms/ml), the level of DAG was 200% over that of the control and
similar to that observed with 2 units/ml thrombin (201% over that of the
control). Therefore, as it appears to be true for thrombin, platelet
response upon binding of anti-p24/CD9 is primarily mediated by the
activation of phospholipase C. When platelets pretreated with aspirin (200
microM) and apyrase (1 mg/ml) were subsequently exposed to anti-p24/CD9,
aggregation still occurred. This indicates that neither secreted ADP nor
thromboxane generation is required for this aggregation response. Using
indo-1 and ratio cytofluorometry, we observed that an increase in platelet
cytosolic calcium is a relatively early event and occurs in either the
presence or absence of calcium in the external media. Phosphorylation
studies of platelet proteins showed that anti-p24/CD9 binding to platelets
caused increased phosphorylation of four proteins with apparent molecular
masses of 50,000, 47,000, 36,000, and 20,000 daltons. These studies suggest
that platelet activation mediated by the surface protein p24/CD9 is mainly
through the stimulation of a phospholipase C, the activation of which is
responsible for the generation of second messengers inositol trisphosphate
and DAG.
The activation of human platelets mediated by anti-human platelet p24/CD9 monoclonal antibodies
Department of Medicine, University of Tennessee, Memphis 38163.
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